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UnknownThe complete chloroplast genome of Epimedium qingchengshanense G. Y. Zhong et B. L. Guo (Berberidaceae), an endangered species endemic to China.
Not available
S-EPMC7748797 | biostudies-literature
TranscriptomicsPhenotypic and transcriptional analysis of the osmotic regulator OmpR in Yersinia pestis
Background The osmotic regulator OmpR in Escherichia coli regulates differentially the expression of major porin proteins OmpF and OmpC. In Yersinia enterocolitica and Y. pseudotuberculosis, OmpR is required for both virulence and survival within macrophages. However, the phenotypic and regulatory r...
ORGANISM(S): Yersinia pestis 
2011-10-23 | E-GEOD-26601 | biostudies-arrayexpress
ProteomicsProteomic analysis of Dpy19l2-deficient human globozoospermia reveals multiple molecular defects
Globozoospermia is a severe teratozoospermia characterized by round-headed spermatozoa without acrosomes, resulting in male infertility. The clinical treatment of globozoospermia involves primarily intracytoplasmic sperm injection because of the low fertilization rate. The deletion of Dpy19l2 is kno...
ORGANISM(S): Homo sapiens (Human) 
2019-08-15 | PXD012302 | Pride
Proteomics Dpy19l2 Human Globozoospermia Round-headed 
MetabolomicsDifferential role of sphingomyelin in influenza virus, rhinovirus and SARS-CoV-2 infection of Calu-3 cells
Host cell lipids play a pivotal role in the pathogenesis of respiratory virus infection. However, a direct comparison of the lipidomic profile of influenza virus and rhinovirus infections is lacking. In this study, we first compared the lipid profile of influenza virus and rhinovirus infection in a ...
2022-11-15 | MTBLS2352 | MetaboLights
UnknownExploring the potential mechanisms of anti-pulmonary fibrosis effects of Luo Han Guo via network pharmacology, molecular docking, and experimental validation.
Not available
S-EPMC12638836 | biostudies-literature
ProteomicsSystematic and quantitative assessment of hydrogen peroxide reactivity with cysteines across human proteomes
Protein cysteinyl residues are the mediators of hydrogen peroxide (H2O2)-dependent redox signaling. However, site-specific mapping of the selectivity and dynamics of these redox reactions in cells poses a major analytical challenge. Here we describe a chemoproteomic platform to systematically and qu...
ORGANISM(S): Homo sapiens (Human) 
2017-08-25 | PXD007153 | Pride
Cysteine chemoproteomics 
UnknownA New Model of Diarrhea with Spleen-Kidney Yang Deficiency Syndrome.
Not available
S-EPMC6186382 | biostudies-literature
ProteomicsDynamic Yin-Yang regulation network of O-GlcNAcylation and phosphorylation mediates vernalization response for flowering in winter wheat
Protein post-translational modification (PTM) increases the functional diversity of the proteome and regulates numerous biological processes in eukaryotes. Two types of PTMs, O-linked-acetyl glucosamine modification (O-GlcNAc) and phosphorylation have been identified on the same amino acid, are cons...
ORGANISM(S): Triticum aestivum (Wheat) 
2020-12-18 | PXD008285 | Pride
Proteomics O-glcnacylation modification Phosphorylation modification 
ProteomicsmiR-29a/b1 regulates the pituitary gland luteinizing hormone secretion and affects mouse ovulation
miR-29a/b1 was reported to be involved in the regulation of reproductive function in female mice, but the underlying molecular mechanisms were not clear. In this study, female mice lacking miR-29a/b1 showed a delay in vaginal opening, irregular estrus cycles, ovulation disorder and infertility. Howe...
ORGANISM(S): Mus musculus (Mouse) 
2021-09-09 | PXD017106 | Pride
Reproduction Knockout Mir-29a/b1 Lh Ovulation 
ProteomicsDynamic Yin-Yang regulation network of O-GlcNAcylation and phosphorylation mediatesvernalization response for flowering in winter wheat, part 2
Protein post-translational modification (PTM) increases the functional diversity of the proteome and regulates numerous biological processes in eukaryotes. Two types of PTMs, O-linked-acetyl glucosamine modification (O-GlcNAc) and phosphorylation have been identified on the same amino acid, are cons...
ORGANISM(S): Triticum aestivum (Wheat) 
2021-05-18 | PXD008298 | Pride
Proteomics O-glcnacylation modification Phosphorylation modification 
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